title: Identification of the apparently essential lysine residues in phospholipase C (Bacillus cereus).
abstract: Phospholipase C (Bacillus cereus) contains two apparently essential and very reactive lysine residues that may be labelled selectively by pyridoxal 5'-phosphate [Aurebekk & Little (1977) Biochem, J. 161, 159--165]. One of these lysine residues was found in the 25-amino acid N-terminal fragment liberated by CNBr digestion of the pyridoxal-labelled enzyme and identified as lysine-6. Two of the labelled peptides isolated from the chymotryptic digest of pyridoxal-labelled enzyme contained proline, suggesting that the other labelled lysine residue is situated in the same region of the primary structure as the single proline residue of the enzyme.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D001409:Bacillus cereus / Q000201:enzymology*; D001665:Binding Sites; D002850:Chromatography, Gel; D002918:Chymotrypsin / Q000378:metabolism; D008239:Lysine / Q000032:analysis*; D010446:Peptide Fragments / Q000032:analysis; D010740:Phospholipases / Q000378:metabolism*; D011732:Pyridoxal Phosphate; D010738:Type C Phospholipases / Q000378:metabolism*
chemical_list: D000596:Amino Acids; D010446:Peptide Fragments; D011732:Pyridoxal Phosphate; D010740:Phospholipases; D010738:Type C Phospholipases; D002918:Chymotrypsin; D008239:Lysine